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P11393

- PHEB_PORPP

UniProt

P11393 - PHEB_PORPP

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Protein

B-phycoerythrin beta chain

Gene

cpeB

Organism
Porphyridium purpureum (Red alga) (Porphyridium cruentum)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei50 – 501Phycourobilin chromophore (covalent; via 2 links)
Binding sitei61 – 611Phycourobilin chromophore (covalent; via 2 links)
Binding sitei82 – 821Phycoerythrobilin chromophore 1 (covalent; via 1 link)
Binding sitei158 – 1581Phycoerythrobilin chromophore 2 (covalent; via 1 link)

GO - Biological processi

  1. oxidation-reduction process Source: UniProtKB-KW
  2. photosynthesis Source: UniProtKB-KW
  3. protein-chromophore linkage Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Electron transport, Photosynthesis, Transport

Keywords - Ligandi

Bile pigment, Chromophore

Names & Taxonomyi

Protein namesi
Recommended name:
B-phycoerythrin beta chain
Gene namesi
Name:cpeB
Encoded oniPlastid; Chloroplast
OrganismiPorphyridium purpureum (Red alga) (Porphyridium cruentum)
Taxonomic identifieri35688 [NCBI]
Taxonomic lineageiEukaryotaRhodophytaBangiophyceaePorphyridialesPorphyridiaceaePorphyridium

Subcellular locationi

Plastidchloroplast thylakoid membrane By similarity; Peripheral membrane protein By similarity; Stromal side By similarity
Note: Forms the periphery of the phycobilisome rod.By similarity

GO - Cellular componenti

  1. chloroplast Source: UniProtKB-KW
  2. phycobilisome Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Membrane, Phycobilisome, Plastid, Thylakoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 177177B-phycoerythrin beta chainPRO_0000199194Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei72 – 721N4-methylasparagine1 Publication

Post-translational modificationi

Contains two covalently linked phycoerythrobilin chromophores and one covalently linked phycourobilin chromophore.

Keywords - PTMi

Methylation

Interactioni

Subunit structurei

Heteropolymer of 6 alpha, 6 beta and one gamma chain.By similarity

Protein-protein interaction databases

IntActiP11393. 1 interaction.
MINTiMINT-8389580.

Structurei

Secondary structure

1
177
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1411Combined sources
Helixi21 – 3212Combined sources
Helixi34 – 4512Combined sources
Helixi48 – 6215Combined sources
Helixi64 – 674Combined sources
Helixi76 – 9924Combined sources
Helixi103 – 1086Combined sources
Turni109 – 1124Combined sources
Helixi113 – 1208Combined sources
Helixi124 – 14219Combined sources
Helixi159 – 17618Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3V57X-ray1.70B/D1-177[»]
3V58X-ray1.85B/D1-177[»]
ProteinModelPortaliP11393.
SMRiP11393. Positions 1-177.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the phycobiliprotein family.Curated

Family and domain databases

Gene3Di1.10.490.20. 1 hit.
InterProiIPR009050. Globin-like.
IPR012128. Phycobilisome_asu/bsu.
[Graphical view]
PfamiPF00502. Phycobilisome. 1 hit.
[Graphical view]
PIRSFiPIRSF000081. Phycocyanin. 1 hit.
SUPFAMiSSF46458. SSF46458. 1 hit.

Sequencei

Sequence statusi: Complete.

P11393-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLDAFSRVVV NSDAKAAYVG GSDLQALKSF IADGNKRLDA VNSIVSNASC
60 70 80 90 100
MVSDAVSGMI CENPGLISPG GNCYTNRRMA ACLRDGEIIL RYVSYALLAG
110 120 130 140 150
DASVLEDRCL NGLKETYIAL GVPTNSSIRA VSIMKAQAVA FITNTATERK
160 170
MSFAAGDCTS LASEVASYFD RVGAAIS
Length:177
Mass (Da):18,554
Last modified:July 1, 1989 - v1
Checksum:i168E71372A29CD89
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti167 – 1671S → Q AA sequence (PubMed:6715353)Curated

Sequence databases

PIRiS02818.
RefSeqiYP_008965770.1. NC_023133.1.

Genome annotation databases

GeneIDi17963946.

Cross-referencesi

Sequence databases

PIRi S02818.
RefSeqi YP_008965770.1. NC_023133.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3V57 X-ray 1.70 B/D 1-177 [» ]
3V58 X-ray 1.85 B/D 1-177 [» ]
ProteinModelPortali P11393.
SMRi P11393. Positions 1-177.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P11393. 1 interaction.
MINTi MINT-8389580.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 17963946.

Family and domain databases

Gene3Di 1.10.490.20. 1 hit.
InterProi IPR009050. Globin-like.
IPR012128. Phycobilisome_asu/bsu.
[Graphical view ]
Pfami PF00502. Phycobilisome. 1 hit.
[Graphical view ]
PIRSFi PIRSF000081. Phycocyanin. 1 hit.
SUPFAMi SSF46458. SSF46458. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "The complete amino-acid sequence of the alpha and beta subunits of B-phycoerythrin from the rhodophytan alga Porphyridium cruentum."
    Sidler W., Kumpf B., Suter F., Klotz A.V., Glazer A.N., Zuber H.
    Biol. Chem. Hoppe-Seyler 370:115-124(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, METHYLATION AT ASN-72.
  2. "Bilin attachment sites in the alpha and beta subunits of B-phycoerythrin. Amino acid sequence studies."
    Lundell D.J., Glazer A.N., DeLange R.J., Brown D.M.
    J. Biol. Chem. 259:5472-5480(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 38-77; 79-84 AND 151-171, CHROMOPHORE ATTACHMENT SITES.

Entry informationi

Entry nameiPHEB_PORPP
AccessioniPrimary (citable) accession number: P11393
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: November 26, 2014
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3